{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078504/MSC1424_README_for-PRIDE-deposition.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078504/checksum.txt"],"Pdf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078504/MSC1424_EV_MS_report.pdf"],"Mztab":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078504/MSC1424_MzTab_TMT-Final.mztab"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078504/MSC1424_RawFiles.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["amahmo4@uic.edu"],"submitter":["Monica Chen"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"software":[""],"submitter_keywords":["Ev","Adipose tissue","Bariatric surgery","Adev","Adiposome"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD078504"],"sample_protocol":["Subcutaneous adipose tissue biopsies were collected from participants before bariatric surgery and approximately 12–14 weeks after surgery. Fresh adipose tissue was rinsed in Medium 199, minced, and digested with Type I collagenase in Medium 199 containing 4% bovine serum albumin. The resulting cell suspension was centrifuged at 500 × g for 1 min to isolate mature adipocytes from the floating layer. Isolated adipocytes were transferred to membrane inserts and maintained in Medium 199 supplemented with 5% exosome-depleted fetal bovine serum and 1% penicillin-streptomycin. Conditioned medium was collected after 24–48 h and subjected to sequential clearing centrifugation steps at 1,000 × g for 5 min and 15,000 × g for 15 min, followed by filtration through a 0.45 µm filter. Adiposomes were pelleted by ultracentrifugation at 150,000 × g for 2 h. The resulting pellets were resuspended and characterized by nanoparticle tracking analysis using a NanoSight NS300 instrument. Vesicle identity and adipocyte-associated origin were assessed by western blotting for extracellular vesicle markers CD9, CD81, and CD63, and adipocyte-associated proteins including PPARγ, adiponectin, and FABP4.  Apolipoprotein B was assessed as a marker of lipoprotein contamination. For proteomic analysis, adiposome proteins were extracted using RIPA buffer and quantified using the Pierce BCA assay. Samples were briefly centrifuged to remove insoluble material, and protein concentrations were further quantified by Qubit. To reduce interference from highly abundant plasma proteins, 300 µg of total protein was incubated with Top14 depletion resin for 15 min and centrifuged. The depleted supernatant was recovered and re-quantified. For each sample, 30 µg of depleted protein was processed using filter-aided sample preparation with 10 kDa molecular weight cutoff filters. Proteins were reduced with 20 mM DTT for 30 min, alkylated with 50 mM iodoacetamide in the dark for 40 min, washed with 8 M urea in 0.1 M ammonium bicarbonate, and digested overnight at 37 °C with trypsin at a 1:30 enzyme-to-protein ratio. Peptides were eluted by centrifugation, rinsed with ammonium bicarbonate and sodium chloride, desalted using Oasis PRiME HLB cartridges, dried, and reconstituted in 5% acetonitrile/0.1% formic acid. Peptide amounts were verified before mass spectrometry. A total of 46 peptide samples, representing paired pre- and post-surgery samples from 23 participants, were processed across TMT10-plex sets. Samples were labeled with TMT10plex reagents according to the manufacturer’s protocol, quenched with hydroxylamine, pooled, desalted, and fractionated by high-pH reversed-phase chromatography on an XBridge BEH C18 column. Concatenated fractions were dried and reconstituted in 5% acetonitrile/0.1% formic acid before LC-MS/MS analysis."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["TMT-labeled peptide fractions were analyzed by liquid chromatography–tandem mass spectrometry using a Q Exactive HF mass spectrometer coupled to an UltiMate 3000 RSLCnano system. Peptides were trapped and then separated on C18 nanoLC columns at 300 nL/min using a 105-min linear gradient with solvent A consisting of 0.1% formic acid in water and solvent B consisting of 0.1% formic acid in 80% acetonitrile. MS1 spectra were acquired at 120,000 resolution across an m/z range of 350–1400. The top 15 precursors with charge states 2–5 were selected for higher-energy collisional dissociation fragmentation using normalized collision energy of 32%, with a dynamic exclusion of 30 s. MS2 scans were acquired at 60,000 resolution. Automatic gain control targets were 3 × 10^6 for MS1 and 1 × 10^5 for MS2, with maximum injection times of 50 ms and 120 ms, respectively. Raw mass spectrometry spectra were searched using Mascot Daemon version 2.6.0 against the UniProt human protein database, version 08/11/2020. The parent ion mass tolerance was set to 10 ppm. Carbamidomethylation of cysteine was specified as a fixed modification, while methionine oxidation and asparagine/glutamine deamidation were specified as variable modifications. Peptide and protein quantification, including TMT reporter ion isotopic purity correction, were performed using Scaffold DDA version 6.0.1. Protein identifications required at least one confident peptide and were filtered at a 5% protein-level false discovery rate."],"omics_type":["Proteomics"],"labhead":["Abeer Mohamed"],"instrument_platform":[""],"labhead_affiliation":["Division of Endocrinology, Diabetes and Metabolism, Department of Medicine, University of Illinois Chicago, Chicago, Illinois, USA"],"submission_type":["COMPLETE"],"species":["Homo Sapiens (human)"],"publication":["42278465 Asada MC, Rakab MS, Mirza I, Scichilone G, Morsy MH, Mostafa A, Bianco FM, Ali MM, Hassan C, Masrur MA, Mahmoud AM. Proteomic Signatures of Adiposomes Track Cardiometabolic Risk Reduction Following Bariatric Surgery. Int J Mol Sci. 2026 27(11):4939 10.3390/ijms27114939"],"submitter_mail":["mchen234@uic.edu"],"submitter_affiliation":["UIC"],"submitter_country":["United States"],"doi":["10.6019/PXD078504"],"pubmed_abstract":["Adipose tissue-derived extracellular vesicles (adiposomes) carry a protein cargo that we previously showed differs between obese and lean individuals. In this study, we investigate how adiposomal protein cargo changes in response to sleeve gastrectomy and examine whether these changes are associated with clinical improvements. Twenty-three obese adults underwent pre- and post-bariatric surgery adipose sampling for adiposome isolation and clinical assessments that included vascular and metabolic profiles and inflammatory markers. The adiposomal protein cargo was analyzed via non-targeted proteomics. Differential protein abundance, pathway enrichment, and correlation analyses were assessed. Twelve weeks after bariatric surgery, BMI and fat mass decreased, accompanied by improved glucose and lipid profiles. Inflammatory markers (leptin, IL-6, CRP) also declined, while adiponectin and nitric oxide increased. Adiposomal proteomics identified 287 proteins, with 138 significantly altered. Downregulated proteins included PRDX2, FN1, SERPIND1, and inflammatory mediators; upregulated proteins included talin-1, fibrinogens, and adiponectin. Correlation analysis linked these changes to improvements in lipid profiles, vascular function, and circulating inflammatory markers. Pathway analysis revealed inhibition of lipid-regulatory pathways alongside enrichment of immune, metabolic, and vascular pathways, including lipoprotein metabolism and endothelial signaling. Bariatric surgery-induced cardiometabolic improvements were accompanied by adiposome proteomic remodeling, characterized by reduced inflammation and metabolic reprogramming."],"pubmed_title":["Proteomic Signatures of Adiposomes Track Cardiometabolic Risk Reduction Following Bariatric Surgery."],"pubmed_authors":["Asada Monica C MC, Rakab Mohamed Saad MS, Mirza Imaduddin I, Scichilone Giorgia G, Morsy Mohammed H MH, Mostafa Amro A, Bianco Francesco M FM, Ali Mohamed M MM, Hassan Chandra C, Masrur Mario A MA, Mahmoud Abeer M AM"],"additional_accession":[]},"is_claimable":false,"name":"Human adipose tissue-derived EV pre- vs post-bariatric surgery (MSC1424: Global protein quantification)","description":"This study investigated longitudinal changes in adipose tissue–derived extracellular vesicle protein cargo, referred to as adiposomes, following bariatric surgery in adults with obesity. 23 adults with obesity scheduled for sleeve gastrectomy were enrolled. Subcutaneous adipose tissue samples and clinical cardiometabolic measurements were collected before surgery and again approximately 12–14 weeks after 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